title: Purification of adenosine deaminase from chicken-egg yolk by affinity column chromatography.
abstract: Adenosine deaminase (adenosine aminohydrolase; E.C. 3.5.4.4) has been purified 4686-fold from egg yolk. The procedure developed was used to isolate the enzyme from eight chicken eggs. An easily prepared affinity column employing purine riboside was used as the final step in the purification. The method developed permits the rapid isolation and a high recovery of the protein. The specific activity of the enzyme preparation obtained is 81.4 mU/mg.
authors.affiliation: Department of Biochemistry and Physiology, Faculty of Chemistry, University of Barcelona, Catalonia, Spain.
authors.forename: R
authors.initials: R
authors.lastname: Lopez
authors.forename: F
authors.initials: F
authors.lastname: Cabre
authors.forename: R
authors.initials: R
authors.lastname: Franco
authors.forename: M
authors.initials: M
authors.lastname: Cascante
authors.forename: E I
authors.initials: EI
authors.lastname: Canela
mesh_terms: D000243:Adenosine Deaminase / Q000032:analysis / Q000302:isolation & purification*; D000818:Animals; D002645:Chickens; D002846:Chromatography, Affinity; D004530:Egg Yolk / Q000032:analysis*
chemical_list: D000243:Adenosine Deaminase